ID A0A0Q5TTJ0_9SPHI Unreviewed; 471 AA.
AC A0A0Q5TTJ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQS39839.1};
GN ORFNames=ASG14_19405 {ECO:0000313|EMBL:KQS39839.1};
OS Pedobacter sp. Leaf194.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS39839.1, ECO:0000313|Proteomes:UP000051708};
RN [1] {ECO:0000313|EMBL:KQS39839.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS39839.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS39839.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS39839.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQS39839.1}.
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DR EMBL; LMPU01000003; KQS39839.1; -; Genomic_DNA.
DR RefSeq; WP_056870392.1; NZ_LMPU01000003.1.
DR AlphaFoldDB; A0A0Q5TTJ0; -.
DR STRING; 1736297.ASG14_19405; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000051708; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
FT DOMAIN 41..220
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 471 AA; 51249 MW; E65167DC9B2C61F4 CRC64;
MNFTKITPDI LAEIKLAIGE ENVFTDAESL DSYSHDETED LRYQPEIVVK PVSPEDISAI
LKICNAHHVP VTPRGGGTGL SGAALPIYGG VSLSMERFKA IIDIDTENLQ ATVEPGVITE
EFINAVGEKG LLYPVDPSSK GSCFIGGNVA HGSGGPRVVK YGTIREYILN LEVVLPNGEI
IWTGANTLKY ASGYNLTQLM IGSEGTLGVV TKIVTKLLPK PSQSVLMMGS FNTNEDACAA
VSAIFRAGVT PSALEFMERK GVEWVIQFDD IKFDLKDDVA ALLMIEFDGD DLDDIFKNCE
KTNLVLEEHK CTEVLFADTA AQKEELWRMR RTMAESVKSN SVYKEEDTVV PRAALPKLIN
GIKQIGGKYG FESVCYGHAG DGNLHVNIIK AGMSDGDWKD KLKFGIAEIF ELTTALGGTL
SGEHGIGLVQ KEFMPIKYSE IHLNLMRGIK NVFDPNGILN PGKIMPDAVN I
//
